5ybl
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AusE== | |
| + | <StructureSection load='5ybl' size='340' side='right'caption='[[5ybl]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ybl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans_FGSC_A4 Aspergillus nidulans FGSC A4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YBL FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.108Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ybl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybl OCA], [https://pdbe.org/5ybl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ybl RCSB], [https://www.ebi.ac.uk/pdbsum/5ybl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AUSE_EMENI AUSE_EMENI] Dioxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). AusE catalyzes various oxidation reactions in addition to spiro-ring formation and works iteratively in the biosynthetic process to produce shunt products such as 5-hydroxyberkeleyone, preaustinoid C and austinoid C (PubMed:23865690).<ref>PMID:22234162</ref> <ref>PMID:22329759</ref> <ref>PMID:23865690</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus nidulans FGSC A4]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Nakashima Y]] | ||
| + | [[Category: Senda M]] | ||
Current revision
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AusE
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